| Value |
3
hours
|
| Organism |
Chicken Gallus gallus |
| Reference |
Massoulié J, Pezzementi L, Bon S, Krejci E, Vallette FM. Molecular and cellular biology of cholinesterases. Prog Neurobiol. 1993 Jul41(1):31-91 p.60 right column bottom paragraphPubMed ID8321908
|
| Primary Source |
Rotundo RL, Fambrough DM. Synthesis, transport and fate of acetylcholinesterase in cultured chick embryos muscle cells. Cell. 1980 Nov22(2 Pt 2):583-94 AND Rotundo RL, Fambrough DM. Secretion of acetylcholinesterase: relation to acetylcholine receptor metabolism. Cell. 1980 Nov22(2 Pt 2):595-602PubMed ID7448873, 7448874
|
| Method |
Abstract of 2nd primary source: "[Investigators] have studied the transport and externalization of these two proteins [Acetylcholinesterase (AChE) and acetylcholine receptors (AChR)] in the same cells using several compounds known to affect secretory processes: colchicine, tunicamycin and the ionophores X-537A, Nigericin and Monensin." |
| Comments |
P.60 right column bottom paragraph: "In cultured chick muscle cells, intracellular AChE was found to turn over much faster than extracellular ACHE, with half-lives of 2-3 hr and 50 hr, respectively, i.e. similar to those found for G1 and G4 in the T28 cells. In addition, the delay between the synthesis and secretion of catalytically active enzyme was 3 hr in these cells (primary sources)." |
| Entered by |
Uri M |
| ID |
115062 |